RNT1_ASPOR
ID RNT1_ASPOR Reviewed; 130 AA.
AC P00651; Q2U194;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Guanyl-specific ribonuclease T1;
DE Short=RNase T1;
DE EC=4.6.1.24;
DE Flags: Precursor;
GN Name=rntA; ORFNames=AO090011000118;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=8534978; DOI=10.1271/bbb.59.1869;
RA Fujii T., Yamaoka H., Gomi K., Kitamoto K., Kumagai C.;
RT "Cloning and nucleotide sequence of the ribonuclease T1 gene (rntA) from
RT Aspergillus oryzae and its expression in Saccharomyces cerevisiae and
RT Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 59:1869-1874(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [3]
RP PROTEIN SEQUENCE OF 27-130.
RX PubMed=5144355; DOI=10.1093/oxfordjournals.jbchem.a129724;
RA Takahashi K.;
RT "The structure and function of ribonuclease T1. XVII. Isolation and amino
RT acid sequences of papain and subtilisin peptides from ribonuclease T1
RT -- the complete covalent structure of ribonuclease T1.";
RL J. Biochem. 70:945-960(1971).
RN [4]
RP SEQUENCE REVISION TO 97-99.
RX PubMed=3936843; DOI=10.1093/oxfordjournals.jbchem.a135339;
RA Takahashi K.;
RT "A revision and confirmation of the amino acid sequence of ribonuclease
RT T1.";
RL J. Biochem. 98:815-817(1985).
RN [5]
RP ACTIVE SITE.
RX PubMed=6061414; DOI=10.1016/s0021-9258(18)99511-6;
RA Takahashi K., Stein W.H., Moore S.;
RT "The identification of a glutamic acid residue as part of the active site
RT of ribonuclease T-1.";
RL J. Biol. Chem. 242:4682-4690(1967).
RN [6]
RP ACTIVE SITE.
RX PubMed=5550972; DOI=10.1093/oxfordjournals.jbchem.a129471;
RA Takahashi K.;
RT "The structure and function of ribonuclease T1. XII. Further studies on
RT rose bengal-catalyzed photooxidation of ribonuclease T1 -- identification
RT of a critical histidine residue.";
RL J. Biochem. 69:331-338(1971).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2844811; DOI=10.1016/s0021-9258(19)37597-0;
RA Arni R., Heinemann U., Tokuoka R., Saenger W.;
RT "Three-dimensional structure of the ribonuclease T1 2'-GMP complex at 1.9-A
RT resolution.";
RL J. Biol. Chem. 263:15358-15368(1988).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=2541256; DOI=10.1016/0022-2836(89)90495-6;
RA Koepke J., Maslowska M., Heinemann U., Saenger W.;
RT "Three-dimensional structure of ribonuclease T1 complexed with guanylyl-
RT 2',5'-guanosine at 1.8-A resolution.";
RL J. Mol. Biol. 206:475-488(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT TRP-71.
RX PubMed=1311385; DOI=10.1016/0022-2836(92)90259-m;
RA Hakoshima T., Itoh T., Tomita K., Goda K., Nishikawa S., Morioka H.,
RA Uesugi S., Ohtsuka E., Ikehara M.;
RT "Three-dimensional structure of a mutant ribonuclease T1 (Y45W) complexed
RT with non-cognizable ribonucleotide, 2'AMP, and its comparison with a
RT specific complex with 2'GMP.";
RL J. Mol. Biol. 223:1013-1028(1992).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=9546218; DOI=10.1038/nsb0498-280;
RA Zegers I., Loris R., Dehollander G., Fattah Haikal A., Poortmans F.,
RA Steyaert J., Wyns L.;
RT "Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed
RT by time-resolved crystallography.";
RL Nat. Struct. Biol. 5:280-283(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10029539; DOI=10.1021/bi982612q;
RA Arni R.K., Watanabe L., Ward R.J., Kreitman R.J., Kumar K., Walz F.G. Jr.;
RT "Three-dimensional structure of ribonuclease T1 complexed with an isosteric
RT phosphonate substrate analogue of GpU: alternate substrate binding modes
RT and catalysis.";
RL Biochemistry 38:2452-2461(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=10211818; DOI=10.1110/ps.8.4.722;
RA Langhorst U., Loris R., Denisov V.P., Doumen J., Roose P., Maes D.,
RA Halle B., Steyaert J.;
RT "Dissection of the structural and functional role of a conserved hydration
RT site in RNase T1.";
RL Protein Sci. 8:722-730(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=12122018; DOI=10.1074/jbc.m206461200;
RA Mignon P., Steyaert J., Loris R., Geerlings P., Loverix S.;
RT "A nucleophile activation dyad in ribonucleases. A combined X-ray
RT crystallographic/ab initio quantum chemical study.";
RL J. Biol. Chem. 277:36770-36774(2002).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=3143569; DOI=10.1111/j.1432-1033.1988.tb14406.x;
RA Hoffmann E., Rueterjans H.;
RT "Two-dimensional 1H-NMR investigation of ribonuclease T1. Resonance
RT assignments, secondary and low-resolution tertiary structures of
RT ribonuclease T1.";
RL Eur. J. Biochem. 177:539-560(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.24;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/RT1/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D28341; BAA05707.1; -; Genomic_DNA.
DR EMBL; D49428; BAA08407.1; -; mRNA.
DR EMBL; AP007171; BAE64671.1; -; Genomic_DNA.
DR PIR; JC4325; NRAST1.
DR RefSeq; XP_001825804.1; XM_001825752.2.
DR PDB; 1B2M; X-ray; 2.00 A; A/B=27-130.
DR PDB; 1BIR; X-ray; 1.80 A; A/B=27-130.
DR PDB; 1BU4; X-ray; 1.90 A; A=27-130.
DR PDB; 1BVI; X-ray; 1.90 A; A/B/C/D=27-130.
DR PDB; 1CH0; X-ray; 2.30 A; A/B/C=27-130.
DR PDB; 1DET; X-ray; 1.80 A; A=27-130.
DR PDB; 1FYS; X-ray; 2.00 A; A=27-130.
DR PDB; 1FZU; X-ray; 1.80 A; A=27-130.
DR PDB; 1G02; X-ray; 1.86 A; A=27-130.
DR PDB; 1GSP; X-ray; 2.20 A; A=27-130.
DR PDB; 1HYF; X-ray; 1.70 A; A=27-130.
DR PDB; 1HZ1; X-ray; 1.80 A; A=27-130.
DR PDB; 1I0V; X-ray; 1.23 A; A=27-130.
DR PDB; 1I0X; X-ray; 1.65 A; A/B/C/D=27-130.
DR PDB; 1I2E; X-ray; 1.80 A; A=27-130.
DR PDB; 1I2F; X-ray; 1.95 A; A=27-130.
DR PDB; 1I2G; X-ray; 1.85 A; A=27-130.
DR PDB; 1I3F; X-ray; 2.35 A; A=27-130.
DR PDB; 1I3I; X-ray; 1.76 A; A=27-130.
DR PDB; 1IYY; NMR; -; A=27-130.
DR PDB; 1LOV; X-ray; 1.55 A; A=27-130.
DR PDB; 1LOW; X-ray; 1.90 A; A=27-130.
DR PDB; 1LOY; X-ray; 1.55 A; A=27-130.
DR PDB; 1LRA; X-ray; 1.90 A; A=27-130.
DR PDB; 1Q9E; X-ray; 1.70 A; A/B/C=27-130.
DR PDB; 1RGA; X-ray; 1.70 A; A=27-130.
DR PDB; 1RGC; X-ray; 2.00 A; A/B=27-130.
DR PDB; 1RGK; X-ray; 1.87 A; A=27-130.
DR PDB; 1RGL; X-ray; 2.00 A; A=27-130.
DR PDB; 1RHL; X-ray; 1.95 A; A=27-130.
DR PDB; 1RLS; X-ray; 1.90 A; A=27-130.
DR PDB; 1RN1; X-ray; 1.84 A; A/B/C=27-130.
DR PDB; 1RN4; X-ray; 1.80 A; A=27-130.
DR PDB; 1RNT; X-ray; 1.90 A; A=27-130.
DR PDB; 1TRP; X-ray; 2.40 A; A/B=27-130.
DR PDB; 1TRQ; X-ray; 2.30 A; A/B=27-130.
DR PDB; 1TTO; X-ray; 2.10 A; A/B/C=27-130.
DR PDB; 1YGW; NMR; -; A=27-130.
DR PDB; 2AAD; X-ray; 2.00 A; A/B=27-130.
DR PDB; 2AAE; X-ray; 1.80 A; A=27-130.
DR PDB; 2BIR; X-ray; 2.30 A; A=27-130.
DR PDB; 2BU4; X-ray; 1.95 A; A=27-130.
DR PDB; 2GSP; X-ray; 1.80 A; A=27-130.
DR PDB; 2HOH; X-ray; 1.90 A; A/B/C/D=27-130.
DR PDB; 2RNT; X-ray; 1.80 A; A=27-130.
DR PDB; 3BIR; X-ray; 1.80 A; A=27-130.
DR PDB; 3BU4; X-ray; 1.77 A; A=27-130.
DR PDB; 3GSP; X-ray; 1.90 A; A=27-130.
DR PDB; 3HOH; X-ray; 1.95 A; A/B/C/D=27-130.
DR PDB; 3RNT; X-ray; 1.80 A; A=27-130.
DR PDB; 3SYU; X-ray; 1.95 A; A=27-130.
DR PDB; 3URP; X-ray; 3.19 A; A=27-130.
DR PDB; 4BIR; X-ray; 1.70 A; A=27-130.
DR PDB; 4BU4; X-ray; 1.80 A; A=27-130.
DR PDB; 4GSP; X-ray; 1.65 A; A=27-130.
DR PDB; 4HOH; X-ray; 2.05 A; A/B/C/D=27-130.
DR PDB; 4ODK; X-ray; 1.40 A; B/C=59-73.
DR PDB; 4RNT; X-ray; 2.20 A; A=27-130.
DR PDB; 5BIR; X-ray; 2.00 A; A/B=27-130.
DR PDB; 5BU4; X-ray; 1.77 A; A=27-130.
DR PDB; 5GSP; X-ray; 1.80 A; A=27-130.
DR PDB; 5HOH; X-ray; 2.00 A; A/B/C/D=27-130.
DR PDB; 5RNT; X-ray; 3.20 A; A=27-130.
DR PDB; 6GSP; X-ray; 2.20 A; A=27-130.
DR PDB; 6RNT; X-ray; 1.80 A; A=27-130.
DR PDB; 7GSP; X-ray; 2.00 A; A/B=27-130.
DR PDB; 7RNT; X-ray; 1.90 A; A=27-130.
DR PDB; 8RNT; X-ray; 1.80 A; A=27-130.
DR PDB; 9RNT; X-ray; 1.50 A; A=27-130.
DR PDBsum; 1B2M; -.
DR PDBsum; 1BIR; -.
DR PDBsum; 1BU4; -.
DR PDBsum; 1BVI; -.
DR PDBsum; 1CH0; -.
DR PDBsum; 1DET; -.
DR PDBsum; 1FYS; -.
DR PDBsum; 1FZU; -.
DR PDBsum; 1G02; -.
DR PDBsum; 1GSP; -.
DR PDBsum; 1HYF; -.
DR PDBsum; 1HZ1; -.
DR PDBsum; 1I0V; -.
DR PDBsum; 1I0X; -.
DR PDBsum; 1I2E; -.
DR PDBsum; 1I2F; -.
DR PDBsum; 1I2G; -.
DR PDBsum; 1I3F; -.
DR PDBsum; 1I3I; -.
DR PDBsum; 1IYY; -.
DR PDBsum; 1LOV; -.
DR PDBsum; 1LOW; -.
DR PDBsum; 1LOY; -.
DR PDBsum; 1LRA; -.
DR PDBsum; 1Q9E; -.
DR PDBsum; 1RGA; -.
DR PDBsum; 1RGC; -.
DR PDBsum; 1RGK; -.
DR PDBsum; 1RGL; -.
DR PDBsum; 1RHL; -.
DR PDBsum; 1RLS; -.
DR PDBsum; 1RN1; -.
DR PDBsum; 1RN4; -.
DR PDBsum; 1RNT; -.
DR PDBsum; 1TRP; -.
DR PDBsum; 1TRQ; -.
DR PDBsum; 1TTO; -.
DR PDBsum; 1YGW; -.
DR PDBsum; 2AAD; -.
DR PDBsum; 2AAE; -.
DR PDBsum; 2BIR; -.
DR PDBsum; 2BU4; -.
DR PDBsum; 2GSP; -.
DR PDBsum; 2HOH; -.
DR PDBsum; 2RNT; -.
DR PDBsum; 3BIR; -.
DR PDBsum; 3BU4; -.
DR PDBsum; 3GSP; -.
DR PDBsum; 3HOH; -.
DR PDBsum; 3RNT; -.
DR PDBsum; 3SYU; -.
DR PDBsum; 3URP; -.
DR PDBsum; 4BIR; -.
DR PDBsum; 4BU4; -.
DR PDBsum; 4GSP; -.
DR PDBsum; 4HOH; -.
DR PDBsum; 4ODK; -.
DR PDBsum; 4RNT; -.
DR PDBsum; 5BIR; -.
DR PDBsum; 5BU4; -.
DR PDBsum; 5GSP; -.
DR PDBsum; 5HOH; -.
DR PDBsum; 5RNT; -.
DR PDBsum; 6GSP; -.
DR PDBsum; 6RNT; -.
DR PDBsum; 7GSP; -.
DR PDBsum; 7RNT; -.
DR PDBsum; 8RNT; -.
DR PDBsum; 9RNT; -.
DR AlphaFoldDB; P00651; -.
DR BMRB; P00651; -.
DR SMR; P00651; -.
DR BindingDB; P00651; -.
DR ChEMBL; CHEMBL1075043; -.
DR CarbonylDB; P00651; -.
DR EnsemblFungi; BAE64671; BAE64671; AO090011000118.
DR GeneID; 5997907; -.
DR KEGG; aor:AO090011000118; -.
DR VEuPathDB; FungiDB:AO090011000118; -.
DR HOGENOM; CLU_111658_1_0_1; -.
DR OMA; CGSVCYW; -.
DR BRENDA; 4.6.1.24; 522.
DR SABIO-RK; P00651; -.
DR EvolutionaryTrace; P00651; -.
DR PRO; PR:P00651; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR InterPro; IPR016191; Ribonuclease/ribotoxin.
DR Pfam; PF00545; Ribonuclease; 1.
DR PIRSF; PIRSF037430; RNase_U2; 1.
DR SUPFAM; SSF53933; SSF53933; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Lyase; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:5144355"
FT CHAIN 27..130
FT /note="Guanyl-specific ribonuclease T1"
FT /id="PRO_0000030833"
FT ACT_SITE 66
FT /evidence="ECO:0000269|PubMed:2844811"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:2844811"
FT ACT_SITE 118
FT /note="Proton donor"
FT DISULFID 28..36
FT /evidence="ECO:0000269|PubMed:5144355"
FT DISULFID 32..129
FT /evidence="ECO:0000269|PubMed:5144355"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1I0V"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:1I0V"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1RHL"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2BIR"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1I0V"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4RNT"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1RN4"
SQ SEQUENCE 130 AA; 13960 MW; 3F49EF41E85E230A CRC64;
MMYSKLLTLT TLLLPTALAL PSLVERACDY TCGSNCYSSS DVSTAQAAGY QLHEDGETVG
SNSYPHKYNN YEGFDFSVSS PYYEWPILSS GDVYSGGSPG ADRVVFNENN QLAGVITHTG
ASGNNFVECT
